Evidence map›Paper›PMID 26048883›Full record

ArticlePlant physiology2015

Subfamily-Specific Fluorescent Probes for Cysteine Proteases Display Dynamic Protease Activities during Seed Germination.

Haibin Lu, Balakumaran Chandrasekar, Julian Oeljeklaus, Johana C Misas-Villamil, Zheming Wang, Takayuki Shindo, Matthew Bogyo, Markus Kaiser, Renier A L van der Hoorn

RetractedErratum issuedOpen access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
12.4field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Insights on the Proteases Involved in Barley and Wheat Grain Germination.International journal of molecular sciences · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Ten Prominent Host Proteases in Plant-Pathogen Interactions.International journal of molecular sciences · 2018
    Review
  15. Article
  16. Article
  17. Article
  18. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 3 countries.

Haibin LuPlant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (H.L., B.C., J.C.M.-V., R.A.L.v.d.H.);Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany (H.L., B.C., J.C.M.-V., T.S., R.A.L.v.d.H.);Center for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany (J.O., Z.W., M.K.); andDepartment of Pathology, Stanford School for Medicine, Stanford, California 94305-5324 (M.B.).
Balakumaran ChandrasekarPlant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (H.L., B.C., J.C.M.-V., R.A.L.v.d.H.);Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany (H.L., B.C., J.C.M.-V., T.S., R.A.L.v.d.H.);Center for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany (J.O., Z.W., M.K.); andDepartment of Pathology, Stanford School for Medicine, Stanford, California 94305-5324 (M.B.).
Julian OeljeklausPlant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (H.L., B.C., J.C.M.-V., R.A.L.v.d.H.);Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany (H.L., B.C., J.C.M.-V., T.S., R.A.L.v.d.H.);Center for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany (J.O., Z.W., M.K.); andDepartment of Pathology, Stanford School for Medicine, Stanford, California 94305-5324 (M.B.).
Johana C Misas-VillamilPlant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (H.L., B.C., J.C.M.-V., R.A.L.v.d.H.);Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany (H.L., B.C., J.C.M.-V., T.S., R.A.L.v.d.H.);Center for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany (J.O., Z.W., M.K.); andDepartment of Pathology, Stanford School for Medicine, Stanford, California 94305-5324 (M.B.).
Zheming WangPlant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (H.L., B.C., J.C.M.-V., R.A.L.v.d.H.);Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany (H.L., B.C., J.C.M.-V., T.S., R.A.L.v.d.H.);Center for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany (J.O., Z.W., M.K.); andDepartment of Pathology, Stanford School for Medicine, Stanford, California 94305-5324 (M.B.).
Takayuki ShindoPlant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (H.L., B.C., J.C.M.-V., R.A.L.v.d.H.);Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany (H.L., B.C., J.C.M.-V., T.S., R.A.L.v.d.H.);Center for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany (J.O., Z.W., M.K.); andDepartment of Pathology, Stanford School for Medicine, Stanford, California 94305-5324 (M.B.).
Matthew BogyoPlant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (H.L., B.C., J.C.M.-V., R.A.L.v.d.H.);Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany (H.L., B.C., J.C.M.-V., T.S., R.A.L.v.d.H.);Center for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany (J.O., Z.W., M.K.); andDepartment of Pathology, Stanford School for Medicine, Stanford, California 94305-5324 (M.B.).
Markus KaiserPlant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (H.L., B.C., J.C.M.-V., R.A.L.v.d.H.);Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany (H.L., B.C., J.C.M.-V., T.S., R.A.L.v.d.H.);Center for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany (J.O., Z.W., M.K.); andDepartment of Pathology, Stanford School for Medicine, Stanford, California 94305-5324 (M.B.).
Renier A L van der HoornPlant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (H.L., B.C., J.C.M.-V., R.A.L.v.d.H.);Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany (H.L., B.C., J.C.M.-V., T.S., R.A.L.v.d.H.);Center for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45117 Essen, Germany (J.O., Z.W., M.K.); andDepartment of Pathology, Stanford School for Medicine, Stanford, California 94305-5324 (M.B.) renier.vanderhoorn@plants.ox.ac.uk.
University of Oxford · GBUniversity of Duisburg-Essen · DEMax Planck Institute for Plant Breeding Research · DEStanford Medicine · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cysteine proteases are an important class of enzymes implicated in both developmental and defense-related programmed cell death and other biological processes in plants. Because there are dozens of cysteine proteases that are posttranslationally regulated by processing, environmental conditions, and inhibitors, new methodologies are required to study these pivotal enzymes individually. Here, we introduce fluorescence activity-based probes that specifically target three distinct cysteine protease subfamilies: aleurain-like proteases, cathepsin B-like proteases, and vacuolar processing enzymes. We applied protease activity profiling with these new probes on Arabidopsis (Arabidopsis thaliana) protease knockout lines and agroinfiltrated leaves to identify the probe targets and on other plant species to demonstrate their broad applicability. These probes revealed that most commercially available protease inhibitors target unexpected proteases in plants. When applied on germinating seeds, these probes reveal dynamic activities of aleurain-like proteases, cathepsin B-like proteases, and vacuolar processing enzymes, coinciding with the remobilization of seed storage proteins.

Indexed as

ArabidopsisCysteine EndopeptidasesCysteine ProteasesFluorescent DyesGerminationModels, ChemicalMolecular StructureMutationNicotianaPhylogenyPlant ProteinsPlants, Genetically ModifiedSeedsCysteine EndopeptidasesCysteine ProteasesFluorescent DyesPlant Proteinsvacuolar processing enzyme

Identifiers

PMID26048883
PMCPMC4528725
OpenAlexW1949572203

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.